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The elution profile of solubilized rat glomerular membranes from a gel filtration column showed two peaks of 125I-ANF (atrial natriuretic factor) binding (367 +/- 21, 156 +/- 12 KDa). Over 85% of the total binding for the extract was in the 367 KDa peak. Guanylate cyclase activity was correlated with 125I-ANF specific binding. ANF activation of guanylate cyclase was also observed. As observed previously with particulate membrane, Scatchard-analysis of ANF binding data with the solubilized extract was consistent with a two-site model. Both affinities (Kd's), 4 pM and 1 nM, are within the range of blood concentrations reported for ANF. These observations suggest that most rat glomerular ANF receptors are large molecular complexes coupled with guanylate cyclase in the 300-350 KDa size range.
M Hamada, and
I J Rondon, and
E D Frohlich, and
F E Cole
January 2010,
Molecular and cellular biochemistry,
M Hamada, and
I J Rondon, and
E D Frohlich, and
F E Cole
June 2010,
The FEBS journal,
M Hamada, and
I J Rondon, and
E D Frohlich, and
F E Cole
July 1990,
European journal of pharmacology,
M Hamada, and
I J Rondon, and
E D Frohlich, and
F E Cole
October 1987,
Regulatory peptides,
M Hamada, and
I J Rondon, and
E D Frohlich, and
F E Cole
June 2005,
Peptides,
M Hamada, and
I J Rondon, and
E D Frohlich, and
F E Cole
July 1990,
Gastroenterology,
M Hamada, and
I J Rondon, and
E D Frohlich, and
F E Cole
April 1988,
The Biochemical journal,
M Hamada, and
I J Rondon, and
E D Frohlich, and
F E Cole
May 1986,
The Journal of biological chemistry,
M Hamada, and
I J Rondon, and
E D Frohlich, and
F E Cole
May 1988,
Science (New York, N.Y.),
M Hamada, and
I J Rondon, and
E D Frohlich, and
F E Cole
April 2009,
Molecular and cellular biochemistry,
